Peptide bond formation on the surface of activated alumina:: peptide chain elongation

被引:26
作者
Bujdák, J [1 ]
Rode, BM
机构
[1] Slovak Acad Sci, Inst Inorgan Chem, Bratislava 84536, Slovakia
[2] Univ Innsbruck, Inst Gen Inorgan & Theoret Chem, A-6020 Innsbruck, Austria
关键词
peptide bond formation; activated alumina; amino acids; chemical evolution;
D O I
10.1023/B:CATL.0000007148.33571.f7
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Reactions of the dipeptides dGly(2), Ala(2)) themselves and in combination with amino acids ( AA) ( glycine, alanine, valine, leucine, proline) and glycine oligopeptides (Gly(3), Gly(4), Gly(5)) on activated alumina surface were investigated. Reactions of glycine oligopeptides led to the formation of longer-chain oligomers up to Gly(11). Combinations of Gly(2) with other amino acids led to various reactions proceeding by different reaction mechanisms. In the reactions of Gly(2) with AA, cyclic anhydride (cyc(Gly(2))) formation was followed by AA addition and molecular rearrangement leading to the formation of Gly-Gly-AA tripeptides. In the reaction of Ala(2) with glycine, this type of reaction apparently does not proceed readily, although very high yields of cyc(Ala(2)) are formed. The reactivities of the individual components are not always reflected in reactions of their mixtures.
引用
收藏
页码:149 / 154
页数:6
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